Characterization of an acid-labile, thermostable β-glycosidase from Thermoplasma acidophilum

被引：0
作者：
Hye-Jung Kim
Ah-Reum Park
Jung-Kul Lee
Deok-Kun Oh
机构：
[1] Konkuk University,Department of Bioscience and Biotechnology
[2] Konkuk University,Department of Chemical Engineering
来源：
Biotechnology Letters | 2009年 / 31卷
关键词：
Characterization; -Glycosidase; pH-sensitive enzyme; Thermostable enzyme;
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摘要：
A recombinant putative β-galactosidase from Thermoplasma acidophilum was purified as a single 57 kDa band of 82 U mg−1. The molecular mass of the native enzyme was 114 kDa as a dimer. Maximum activity was observed at pH 6.0 and 90°C. The enzyme was unstable below pH 6.0: at pH 6 its half-life at 75°C was 28 days but at pH 4.5 was only 13 h. Catalytic efficiencies decreased as p-nitrophenyl(pNP)-β-d-fucopyranoside (1067) > pNP-β-d-glucopyranoside (381) > pNP-β-d-galactopyranoside (18) > pNP-β-d-mannopyranoside (11 s−1 mM−1), indicating that the enzyme was a β-glycosidase.
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